glyoxal has been researched along with serine in 5 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 2 (40.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 1 (20.00) | 29.6817 |
2010's | 2 (40.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Ibuki, F; Tashiro, M; Yamada, H; Yamada, M; Yamaguchi, H | 1 |
Cohen, AB | 1 |
Cosgrove, S; Hewage, C; Malthouse, JP; Rogers, L; Spink, E | 1 |
Howe, N; Malthouse, JP; O'Donohoe, CA; Petrillo, T | 1 |
Cleary, JA; Doherty, W; Evans, P; Malthouse, JP | 1 |
5 other study(ies) available for glyoxal and serine
Article | Year |
---|---|
The reactive site of eggplant trypsin inhibitor.
Topics: Anhydrides; Arginine; Binding Sites; Carboxypeptidases; Cyclohexanones; Disulfides; Glyoxal; Hydrogen-Ion Concentration; Plants; Serine; Trinitrobenzenesulfonic Acid; Trypsin Inhibitors | 1976 |
Mechanism of action of alpha-1-antitrypsin.
Topics: alpha 1-Antitrypsin; Amino Acids; Anilides; Arginine; Aspartic Acid; Benzoates; Binding Sites; Binding, Competitive; Cholinesterase Inhibitors; Chymotrypsin; Fibrinolysin; Glyoxal; Histidine; Isoflurophate; Leucine; Lysine; Nitro Compounds; Pancreatic Elastase; Peptide Hydrolases; Protease Inhibitors; Serine; Structure-Activity Relationship; Subtilisins; Thrombin; Trypsin Inhibitors | 1973 |
13C and 1H NMR studies of ionizations and hydrogen bonding in chymotrypsin-glyoxal inhibitor complexes.
Topics: Animals; Binding Sites; Catalysis; Cattle; Chymotrypsin; Glyoxal; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Ions; Magnetic Resonance Spectroscopy; Serine; Surface Plasmon Resonance; Temperature | 2007 |
Importance of tetrahedral intermediate formation in the catalytic mechanism of the serine proteases chymotrypsin and subtilisin.
Topics: Biocatalysis; Catalytic Domain; Chymotrypsin; Glyoxal; Hydrogen Bonding; Hydrogen-Ion Concentration; Oligopeptides; Protease Inhibitors; Serine; Subtilisin | 2012 |
Hemiacetal stabilization in a chymotrypsin inhibitor complex and the reactivity of the hydroxyl group of the catalytic serine residue of chymotrypsin.
Topics: Animals; Biocatalysis; Catalytic Domain; Cattle; Chymotrypsin; Glyoxal; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Kinetics; Nuclear Magnetic Resonance, Biomolecular; Oligopeptides; Protease Inhibitors; Serine; Solutions; Stereoisomerism; Thermodynamics | 2014 |